O09130 · NF2IP_MOUSE

  • Protein
    NFATC2-interacting protein
  • Gene
    Nfatc2ip
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

In T-helper 2 (Th2) cells, regulates the magnitude of NFAT-driven transcription of a specific subset of cytokine genes, including IL3, IL4, IL5 and IL13, but not IL2. Recruits PRMT1 to the IL4 promoter; this leads to enhancement of histone H4 'Arg-3'-methylation and facilitates subsequent histone acetylation at the IL4 locus, thus promotes robust cytokine expression. Down-regulates formation of poly-SUMO chains by UBE2I/UBC9.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Biological Processpositive regulation of transcription by RNA polymerase II

Names & Taxonomy

Protein names

  • Recommended name
    NFATC2-interacting protein
  • Alternative names
    • 45 kDa NF-AT-interacting protein (45 kDa NFAT-interacting protein)
    • Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein

Gene names

    • Name
      Nfatc2ip
    • Synonyms
      Nip45

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    O09130
  • Secondary accessions
    • Q8CDG2
    • Q9CVY5

Proteomes

Organism-specific databases

Subcellular Location

Note: TRAF1 is associated with a fraction of NFATC2IP in the cytoplasm and prevents its translocation to the nucleus.

Keywords

Phenotypes & Variants

Disruption phenotype

Mutant mice are born at the expected Mendelian ratio and appear healthy and viable. No alteration in thymic T-cell populations, T-cell proliferation, or peripheral lymphocyte development. Inefficient type-2 antiparasitic immune response to the intestinal nematode Trichinella spiralis due to impaired IL4 and IL13 cytokine production by Th2 cells.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 32 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue, cross-link.

TypeIDPosition(s)Description
ChainPRO_00002810091-412NFATC2-interacting protein
Modified residue49Phosphoserine
Modified residue51Phosphoserine
Modified residue79Phosphoserine
Modified residue81Phosphoserine
Modified residue83Phosphoserine
Modified residue118Phosphoserine
Cross-link120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue191Phosphoserine
Modified residue197Phosphoserine
Modified residue307Phosphoserine
Modified residue309Phosphothreonine
Modified residue311Phosphothreonine
Modified residue362Phosphoserine
Modified residue383Phosphoserine

Post-translational modification

Methylation at the N-terminus by PRMT1 modulates interaction with the NFAT complex and results in augmented cytokine production.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Highest level detected in spleen, thymus and testis.

Gene expression databases

Interaction

Subunit

Interacts with NFATC2, TRAF1, TRAF2 and PRMT1. Interacts with UBE2I/UBC9.

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, coiled coil, domain.

TypeIDPosition(s)Description
Region1-38Disordered
Compositional bias12-27Basic residues
Region58-115Disordered
Region136-206Disordered
Compositional bias146-160Polar residues
Compositional bias163-187Basic and acidic residues
Coiled coil168-227
Domain341-412Ubiquitin-like

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    412
  • Mass (Da)
    45,121
  • Last updated
    1997-07-01 v1
  • Checksum
    DD58FE5C7055C186
MAEPLRGRGPRSRGGRGARRARGARGRCPRARQSPARLIPDTVLVDLVSDSDEEVLEVADPVEVPVARLPAPAKPEQDSDSDSEGAAEGPAGAPRTLVRRRRRRLLDPGEAPVVPVYSGKVQSSLNLIPDNSSLLKLCPSEPEDEADLTNSGSSPSEDDALPSGSPWRKKLRKKCEKEEKKMEEFPDQDISPLPQPSSRNKSRKHTEALQKLREVNKRLQDLRSCLSPKQHQSPALQSTDDEVVLVEGPVLPQSSRLFTLKIRCRADLVRLPVRMSEPLQNVVDHMANHLGVSPNRILLLFGESELSPTATPSTLKLGVADIIDCVVLASSSEATETSQELRLRVQGKEKHQMLEISLSPDSPLKVLMSHYEEAMGLSGHKLSFFFDGTKLSGKELPADLGLESGDLIEVWG

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0U1RNY9A0A0U1RNY9_MOUSENfatc2ip110

Sequence caution

The sequence BAB24331.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict2in Ref. 2; BAC26788
Compositional bias12-27Basic residues
Compositional bias146-160Polar residues
Compositional bias163-187Basic and acidic residues
Sequence conflict200in Ref. 2; BAC26788
Sequence conflict390-391in Ref. 2; BAB24331

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U76759
EMBL· GenBank· DDBJ
AAC52963.1
EMBL· GenBank· DDBJ
mRNA
AK005947
EMBL· GenBank· DDBJ
BAB24331.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AK030107
EMBL· GenBank· DDBJ
BAC26788.1
EMBL· GenBank· DDBJ
mRNA
BC113761
EMBL· GenBank· DDBJ
AAI13762.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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